Crystallization and preliminary X-ray diffraction studies of the guanylatekinase-like domain of PSD-95 protein from rat

Citation
Jj. Kim et al., Crystallization and preliminary X-ray diffraction studies of the guanylatekinase-like domain of PSD-95 protein from rat, ACT CRYST D, 57, 2001, pp. 616-617
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
4
Pages
616 - 617
Database
ISI
SICI code
0907-4449(200104)57:<616:CAPXDS>2.0.ZU;2-K
Abstract
The PSD-95 (postsynaptic density-95) protein, one of the members of the MAG UK (membrane-associated guanylate kinase) family, is composed of three PDZ domains, one SH3 domain and one guanylate kinase-like (GK) domain. The GK d omain mediates the scaffolding function of PSD-95 by protein-protein intera ction. Here, the GK domain was subcloned, expressed as an intein fusion pro tein, purified without the intein and then crystallized at room temperature by the hanging-drop vapour-diffusion method using PEG 8000 as a precipitan t. The complete native data set was collected to a resolution of 2.35 Angst rom using flash-cooling. The crystals belong to the primitive tetragonal sp ace group P4(3) (or P4(1)), with unit-cell parameters a = b = 70.03 (4), c = 37.64 (1) Angstrom.